Cathelicidin peptide analogues inhibit EV71 infection through blocking viral entry and uncoating.
Fan. Tingting T; Liu. Bing B; Yao. Haoyan H; Chen. Xinrui X; Yang. Hang H; Guo. Shangrui S; Wu. Bo B; Li. Xiaozhen X; Li. Xinyu X; Xun. Meng M; Wang. Hongliang H
Key Findings
- LL-18 and FF-18 are more effective against EV71 than the parent peptide LL-37
- The peptides bind directly to the virus surface, blocking the virus‑receptor interaction and preventing uncoating
- In animal studies the peptides reduced the harmful effects of EV71 infection
Practical Outcomes
- These findings are interesting but not yet ready for personal use. They suggest that engineered versions of LL-37 could become antiviral tools in the future, but more research on safety, dosing, and delivery is needed before biohackers can apply them.
Summary
Researchers found that two short versions of the natural peptide LL-37, called LL-18 and FF-18, can stop a nasty virus (EV71) from getting into cells and spreading, and they work better than the original peptide in lab and animal tests.
Abstract
Given the serious neurological complications and deaths associated with enterovirus 71 (EV71) infection, there is an urgent need to develop effective antivirals against this viral infection. In this study, we demonstrated that two Cathelicidin-derived peptides, LL-18 and FF-18 were more potent against EV71 infection than the parent peptide LL-37, which is the mature and processed form of Cathelicidin. These peptides could directly bind to the EV71 virus particles, but not to coxsackievirus, indicative of their high specificity. The binding of peptides with the virus surface occupied the viral canyon region in a way that could block virus-receptor interactions and inhibit viral uncoating. In addition, these peptide analogues could also relieve the deleterious effect of EV71 infection in vivo. Therefore, Cathelicidin-derived peptides might be excellent candidates for further development of antivirals to treat EV71 infection.
Study Information
pubmed
2024
2024-01-25T00:00:00.000Z
10.1371/journal.ppat.1011967
11
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